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Phenoloxidase of Mycobacterium leprae [PDF]
INVESTIGATIONS of the metabolism of Mycobacteriumleprae1 have revealed a few of the metabolic characteristics of this micro-organism. Concentrates of M. leprae prepared from lepromatous material actively oxidized 3,4-dihydroxyphenylalanine (DOPA) to pigmented products, in vitro2. Among several strains of mycobactena tested (including M. tuberculosis, M.
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Implications of Chemoautotrophism in Mycobacterium leprae
Nature New Biology, 1973Mycobacterium leprae is generally considered as a host-dependent intracellular parasite, deriving energy and nutrients for growth from the human phagocytic cells in which it multiplies abundantly. This has recently been challenged by Kato1,2 who reported that many characteristics of M. leprae recall those of the chemoautotrophic microorganisms.
A. Donawa+3 more
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Protein antigens of Mycobacterium leprae
Research in Microbiology, 1990Protein antigens of Mycobacterium leprae have been identified by screening the lambda gt11, pYA626 and pHC79::M. leprae genomic libraries with pooled sera from leprosy patients and with antiserum to M. leprae cell wall protein (CWP) aggregate. Immunological screening of the lambda gt11 library with pooled sera from 21 lepromatous (LL) leprosy patients ...
E.F. de Carvalho+6 more
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Study on the micromorphology of Mycobacterium leprae
Archives of Dermatological Research, 1985The micromorphology of Mycobacterium leprae is described. After fixation with osmium tetroxide supplemented with calcium ions, the cell wall was seen to be composed of three layers; the cytoplasmic membrane exhibited the architecture of an elementary membrane. The mesosomes were best visualized after fixation with glutaraldehyde; they were sometimes in
G. D. Burchard, M. Bierther
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Properties of Phenoloxidase in Mycobacterium leprae
Nature, 1968Mycobacterium leprae separated from infected human tissues, oxidizes 3,4-dihydroxyphenylalanine (dopa) and a few other phenolic compounds1–3. This property is not shown by several other mycobacteria1,2,4. Phenoloxidase occurs in vertebrate melanocytes and is widely distributed in the plant kingdom5. (E.C.
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The truncated hemoglobin from Mycobacterium leprae
Biochemical and Biophysical Research Communications, 2002Truncated hemoglobins (trHb's) form a family of low molecular weight O2 binding hemoproteins distributed in eubacteria, protozoa, and plants. TrHb's branch in a distinct clade within the hemoglobin (Hb) superfamily. A unique globin gene has recently been identified from the complete genome sequence of Mycobacterium leprae that is predicted to encode a ...
VISCA P+8 more
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Nitric Oxide and Mycobacterium leprae Pathogenicity
IUBMB Life, 2002AbstractLeprosy is an old, still dreaded infectious disease caused by the obligate intracellular bacterium Mycobacterium leprae . During the infectious process, M. leprae is faced with the host macrophagic environment, where the oxidative stress and NO release, combined with low pH, low pO 2, and high pCO 2, contribute to limit the growth of the ...
VISCA, PAOLO+4 more
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2002
Publisher Summary Mycobacterium leprae (M. leprae) is one of the first organisms to be established as the cause of diseases in humans. In spite of this, it is the least understood of any bacterium of medical importance. All mycobacteria are difficult to work with; the pathogens have to be handled in high-containment facilities, their unusual cell ...
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Publisher Summary Mycobacterium leprae (M. leprae) is one of the first organisms to be established as the cause of diseases in humans. In spite of this, it is the least understood of any bacterium of medical importance. All mycobacteria are difficult to work with; the pathogens have to be handled in high-containment facilities, their unusual cell ...
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Properties of lysophospholipase in Mycobacterium leprae
Journal of Basic Microbiology, 1996AbstractLysophospholipids are key intermediates in the metabolism of phospholipids. Cytoplasmic membranes of both eukaryotes and prokaryotes are made of phospholipid bilayers. Phospholipases are activated during phagocytosis. Lysophospholipids generated by phospholipase A2 or A1 degrade cell membranes and can cause cell lysis.
K. Prabhakaran+2 more
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